ID B0ZCH7_ARATH Unreviewed; 360 AA. AC B0ZCH7; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 24-JAN-2024, entry version 67. DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483}; DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483}; DE Flags: Fragment; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702 {ECO:0000313|EMBL:ABZ04764.1}; RN [1] {ECO:0000313|EMBL:ABZ04764.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=18273534; DOI=10.1007/s00239-007-9063-3; RA Moore R.C., Stevens M.H.H.; RT "Local patterns of nucleotide polymorphism are highly variable in the RT selfing species Arabidopsis thaliana."; RL J. Mol. Evol. 66:116-129(2008). CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|ARBA:ARBA00004906}. CC -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL subfamily. CC {ECO:0000256|ARBA:ARBA00024209}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; EU351820; ABZ04764.1; -; Genomic_DNA. DR AlphaFoldDB; B0ZCH7; -. DR ExpressionAtlas; B0ZCH7; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro. DR CDD; cd16461; RING-H2_EL5-like; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR044600; ATL1/ATL16-like. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR46913:SF16; RING-H2 FINGER PROTEIN ATL1; 1. DR PANTHER; PTHR46913; RING-H2 FINGER PROTEIN ATL16; 1. DR Pfam; PF13639; zf-RING_2; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175}; KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}. FT TRANSMEM 29..52 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 122..164 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT REGION 237..256 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 320..343 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 237..252 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABZ04764.1" FT NON_TER 360 FT /evidence="ECO:0000313|EMBL:ABZ04764.1" SQ SEQUENCE 360 AA; 40179 MW; 9CC40B4FF3C38B3F CRC64; LVFPPPPPPP STTFTSPIFP RTSSSGTSFP ILAIAVIGIL ATAFLLVSYY IFVIKCCLNW HQIDIFRRRR RSSDQNPLMI YSPHEVNRGL DESAIRAIPV FKFKKRDVVA GEEDQSKNSQ ECSVCLNEFQ EDEKLRIIPN CCHVFHIDCI DIWLQGNANC PLCRTSVSCE ASFTLDLISA PSSPRENSPR SRNRNLEPGL VLGGDDDFVV IELGASNGNN RESVRNIDFL TEQERVTSNE VSTGNSPKSV SPLPIKFDNR GMYKKERKFH KVTSMGDECI DTRGKDGHFG EIQPIRRSIS MDSSVDRQLY LAVQEEISRR NRQIPVAGDG EDSSSSGGGN SRVMKRCFFS FGSSRTSKSS //